Globular protein

Although it is still unknown how proteins fold up naturally, new evidence has helped advance understanding.

[3] By the second law of thermodynamics, the free energy difference between unfolded and folded states is contributed by enthalpy and entropy changes.

As the free energy difference in a globular protein that results from folding into its native conformation is small, it is marginally stable, thus providing a rapid turnover rate and effective control of protein degradation and synthesis.

Other globular proteins are the alpha, beta and gamma (IgA, IgD, IgE, IgG and IgM) globulin.

Nearly all enzymes with major metabolic functions are globular in shape, as well as many signal transduction proteins.